Épithélium olfactif

Résumé

thumb|Épithélium olfactif de porc L'épithélium olfactif est une muqueuse de la cavité nasale dont la fonction principale est la détection des molécules odorantes véhiculées par le milieu environnant l'individu (l'air ou l'eau). Il est à différencier de l'épithélium respiratoire qui recouvre le reste de la cavité nasale. Chez l'homme, il occupe une petite surface diffuse au sommet de la cavité nasale, d'environ , soit moins de 8 % de la surface. Seulement 5 à 10 % de l'air inhalé atteint cet épithélium. Chez d'autres espèces comme le rat, qui a un sens de l'odorat beaucoup plus développé, la surface de cet épithélium est plus étendue et occupe la moitié de la cavité nasale Escada P.A., Lima C. and da Silva J.M. (2009). The human olfactory mucosa. Eur. Arch. Otorhinolaryngol. 266: 1675-1680 (, , lisible en ligne, consulté le 11 mars 2020).. Cet épithélium est dit pseudo-stratifié car bien que présentant une seu

Source officielle

https://fr.wikipedia.org/wiki/%C3%89pith%C3%A9lium_olfactif

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EPFL2004

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, , , ,

We have screened an odorant compound library and discovered molecules acting as chemical signals that specifically activate both G-protein-coupled olfactory receptors (ORs) on the cell surface of olfactory sensory neurons and the human nuclear estrogen receptor alpha (ER) involved in transcriptional regulation of cellular differentiation and proliferation in a wide variety of tissues. Hence, these apparent dual active odorants induce distinct signal transduction pathways at different subcellular localizations, which affect both neuronal signaling, resulting in odor perception, and the ER-dependent transcriptional control of specific genes. We demonstrate these effects using fluorescence-based in vitro and cellular assays. Among these odorants, we have identified synthetic sandalwood compounds, an important class of molecules used in the fragrance industry. For one estrogenic odorant we have also identified the cognate OR. This prompted us to compare basic molecular recognition principles of odorants on the two structurally and apparent functionally non-related receptors using computational modeling in combination with functional assays. Faced with the increasing evidence that ORs may perform chemosensory functions in a number of tissues outside of the nasal olfactory epithelium, the unraveling of these molecular ligand-receptor interaction principles is of critical importance. In addition the evidence that certain olfactory sensory neurons naturally co-express ORs and ERs may provide a direct functional link between the olfactory and hormonal systems in humans. Our results are therefore useful for defining the structural and functional characteristics of ER-specific odorants and the role of odorant molecules in cellular processes other than olfaction.

American Society for Biochemistry and Molecular Biology2009

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The Mouse Eugenol Odorant Receptor: Structural and Functional Plasticity of a Broadly Tuned Odorant Binding Pocket

Olivia Baud, Sylvain Etter, Horst Pick, Horst Vogel

Molecular interactions of odorants with their olfactory receptors (ORs) are of central importance for the ability of the mammalian olfactory system to detect and discriminate a vast variety of odors with a limited set of receptors. How a particular OR binds and distinguishes different odorant molecules remains largely unknown on a structural basis. Here we investigated this question for the mouse eugenol receptor (mOR-EG). By screening a large odorant library, we discovered a wide range of chemical structures activating the receptor in heterologous mammalian cells. Potent agonists comprise (i) benzene, (ii) cyclohexane, or (iii) polycyclic structures substituted with alcohol, aldehyde, keto, ether, or esterified carboxylic groups. To detect those amino acids within the receptor that are in contact with a particular bound odorant molecule, we investigated how distinct mOR-EG point mutants were activated by the different odorant agonists found for the wild-type receptor. We identified 11 amino acids as a part of the receptor's ligand binding pocket. Molecular modeling predicted 10 of these residues in transmembrane helices TM3-TM6 and one in the extracellular loop between TM2 and TM3. These amino acids participate in odorant binding with variable importance depending on the type of odorant, revealing functional "fingerprints" of ligand-receptor interactions.

American Chemical Society2011

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